protein-arginine deiminase (PAD) domain-containing protein may catalyze the conversion of protein-bound arginine residues to citrulline residues in a calcium ion-dependent manner
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
283-660
0e+00
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyze the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognized (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localization. The expression of type I PAD is known to be under the control of oestrogen.
:
Pssm-ID: 460794 Cd Length: 393 Bit Score: 685.49 E-value: 0e+00
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
113-273
7.92e-91
Protein-arginine deiminase (PAD) middle domain; This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold.
:
Pssm-ID: 462510 Cd Length: 159 Bit Score: 278.61 E-value: 7.92e-91
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
7-112
5.21e-53
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic domain of protein-arginine deiminase has a cupredoxin-like fold, but lacks the Cu binding site. PAD (protein-arginine deiminase) and protein L-arginine iminohydrolase catalyze the conversion of protein arginine residues to citrulline residues post-translationally in a process called citrullination. The modification plays crucial regulatory roles in development and cell differentiation.
:
Pssm-ID: 259876 Cd Length: 108 Bit Score: 177.57 E-value: 5.21e-53
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
283-660
0e+00
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyze the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognized (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localization. The expression of type I PAD is known to be under the control of oestrogen.
Pssm-ID: 460794 Cd Length: 393 Bit Score: 685.49 E-value: 0e+00
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
113-273
7.92e-91
Protein-arginine deiminase (PAD) middle domain; This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold.
Pssm-ID: 462510 Cd Length: 159 Bit Score: 278.61 E-value: 7.92e-91
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
7-112
5.21e-53
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic domain of protein-arginine deiminase has a cupredoxin-like fold, but lacks the Cu binding site. PAD (protein-arginine deiminase) and protein L-arginine iminohydrolase catalyze the conversion of protein arginine residues to citrulline residues post-translationally in a process called citrullination. The modification plays crucial regulatory roles in development and cell differentiation.
Pssm-ID: 259876 Cd Length: 108 Bit Score: 177.57 E-value: 5.21e-53
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
1-111
1.79e-52
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.
Pssm-ID: 462509 Cd Length: 113 Bit Score: 176.21 E-value: 1.79e-52
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence ...
283-660
0e+00
Protein-arginine deiminase (PAD); Members of this family are found in mammals. In the presence of calcium ions, PAD enzymes EC:3.5.3.15 catalyze the post-translational modification reaction responsible for the formation of citrulline residues: Protein L-arginine + H2O <=> Protein L-citrulline + NH3. Several types are recognized (and included in the family) on the basis of molecular mass, substrate specificity, and tissue localization. The expression of type I PAD is known to be under the control of oestrogen.
Pssm-ID: 460794 Cd Length: 393 Bit Score: 685.49 E-value: 0e+00
Protein-arginine deiminase (PAD) middle domain; This family represents the central ...
113-273
7.92e-91
Protein-arginine deiminase (PAD) middle domain; This family represents the central non-catalytic domain of protein-arginine deiminase. This domain has an immunoglobulin-like fold.
Pssm-ID: 462510 Cd Length: 159 Bit Score: 278.61 E-value: 7.92e-91
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic ...
7-112
5.21e-53
N-terminal non-catalytic domain of protein-arginine deiminase; The N-terminal non-catalytic domain of protein-arginine deiminase has a cupredoxin-like fold, but lacks the Cu binding site. PAD (protein-arginine deiminase) and protein L-arginine iminohydrolase catalyze the conversion of protein arginine residues to citrulline residues post-translationally in a process called citrullination. The modification plays crucial regulatory roles in development and cell differentiation.
Pssm-ID: 259876 Cd Length: 108 Bit Score: 177.57 E-value: 5.21e-53
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal ...
1-111
1.79e-52
Protein-arginine deiminase (PAD) N-terminal domain; This family represents the N-terminal non-catalytic domain of protein-arginine deiminase. This domain has a cupredoxin-like fold.
Pssm-ID: 462509 Cd Length: 113 Bit Score: 176.21 E-value: 1.79e-52
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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